7YQD

EM structure of human PA28gamma (wild-type)

Summary for 7YQD

• Entry DOI: 10.2210/pdb7yqd/pdb
• EMDB information: 34024
• Descriptor: Proteasome activator complex subunit 3 (1 entity in total)
• Functional Keywords: proteasome activator gamma, pa28gamma, psme3, protein transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 7
• Total formula weight: 206829.50

Authors

Chen, D.-D.,Hao, J.,Yun, C.-H. (deposition date: 2022-08-06, release date: 2022-09-21, Last modification date: 2024-07-03)

Primary citation

Chen, D.D.,Hao, J.,Shen, C.H.,Deng, X.M.,Yun, C.H.
Atomic resolution Cryo-EM structure of human proteasome activator PA28 gamma.
Int.J.Biol.Macromol., 219:500-507, 2022

PubMed Abstract: The PA28 family proteasome activators play important roles in regulating proteasome activities. Though the three paralogs (PA28α, PA28β, and PA28γ) are similar in terms of primary sequence, they show significant differences in expression pattern, cellular localization and most importantly, biological functions. While PA28αβ is responsible for promoting peptidase activity of proteasome to facilitate MHC-I antigen processing, but unable to promote protein degradation, PA28γ is well-known to not only promote peptidase activity but also proteolytic activity of proteasome. However, why this paralog has the unique function remains elusive. Previous structural studies have mainly focused on mammalian PA28α, PA28β and PA28αβ heptamers, while structural studies on mammalian PA28γ of atomic resolution are still absent to date. In the present work, we determined the Cryo-EM structure of the human PA28γ heptamer at atomic resolution, revealing interesting unique structural features that may hint our understanding the functional mechanisms of this proteasome activator.

PubMed: 35932807
DOI: 10.1016/j.ijbiomac.2022.07.246

Experimental method

ELECTRON MICROSCOPY (3.4 Å)